the mutant retains catalytic proficiency but is optimally active at more acidic conditions than the wild type enzyme (pH 5.7).The mutation reduces kcat 17fold
the mutant retains catalytic proficiency and is optimally active at wild type conditions. The E86Q mutation rather modestly affects kcat, decreasing it by a factor of 4
site-directed mutagenesis, substrate binding structure and kinetics compared to the wild-type enzyme, the mutant shows highly reduced catalytic activity. The loop mutant fails to induce a conformational change in Arg213
site-directed mutagenesis, substrate binding structure and kinetics compared to the wild-type enzyme, the mutant shows highly reduced catalytic activity
site-directed mutagenesis, methionine is closest in shape to a lysine but cannot form a Schiff base, mutation of Lys170 results in a dramatic loss in reactivity. Comparison of mutant and wild-type crystal structures, the K170M substrate-bound structure reveals that His143 adopts partial occupancies of both of the conformations observed in the wild-type structures, overview
reduced catalytic activity, replacement of Arg23 results in Tyr28 adopting an alternative conformation, more favourable than the one required for catalysis
site-directed mutagenesis, methionine is closest in shape to a lysine but cannot form a Schiff base, mutation of Lys170 results in a dramatic loss in reactivity. Comparison of mutant and wild-type crystal structures, the K170M substrate-bound structure reveals that His143 adopts partial occupancies of both of the conformations observed in the wild-type structures, overview
expression of endogenous DHD/SHD-1 is suppressed by RNAi in transgenic tobacco plants, the transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin, but accumulation of dehydroquinate and shikimate, possibly due to existence of a parallel extra-plastidic shikimate pathway into which dehydroquinate is diverted with a second gene DHD/SHD-2 in tobacco lacking a plastidic targeting sequence, the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway, phenotype, overview
expression of endogenous DHD/SHD-1 is suppressed by RNAi in transgenic tobacco plants, the transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin, but accumulation of dehydroquinate and shikimate, possibly due to existence of a parallel extra-plastidic shikimate pathway into which dehydroquinate is diverted with a second gene DHD/SHD-2 in tobacco lacking a plastidic targeting sequence, the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway, phenotype, overview
expression of endogenous DHD/SHD-1 is suppressed by RNAi in transgenic tobacco plants, the transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin, but accumulation of dehydroquinate and shikimate, possibly due to existence of a parallel extra-plastidic shikimate pathway into which dehydroquinate is diverted with a second gene DHD/SHD-2 in tobacco lacking a plastidic targeting sequence, the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway, phenotype, overview